5ZLI

Crystal structure of glutamine synthetase from helicobacter pylori

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004356	molecular_function	glutamine synthetase activity
A	0005737	cellular_component	cytoplasm
A	0016020	cellular_component	membrane
A	0019740	biological_process	nitrogen utilization
A	1901704	biological_process	L-glutamine biosynthetic process
B	0003824	molecular_function	catalytic activity
B	0004356	molecular_function	glutamine synthetase activity
B	0005737	cellular_component	cytoplasm
B	0016020	cellular_component	membrane
B	0019740	biological_process	nitrogen utilization
B	1901704	biological_process	L-glutamine biosynthetic process
C	0003824	molecular_function	catalytic activity
C	0004356	molecular_function	glutamine synthetase activity
C	0005737	cellular_component	cytoplasm
C	0016020	cellular_component	membrane
C	0019740	biological_process	nitrogen utilization
C	1901704	biological_process	L-glutamine biosynthetic process
D	0003824	molecular_function	catalytic activity
D	0004356	molecular_function	glutamine synthetase activity
D	0005737	cellular_component	cytoplasm
D	0016020	cellular_component	membrane
D	0019740	biological_process	nitrogen utilization
D	1901704	biological_process	L-glutamine biosynthetic process
E	0003824	molecular_function	catalytic activity
E	0004356	molecular_function	glutamine synthetase activity
E	0005737	cellular_component	cytoplasm
E	0016020	cellular_component	membrane
E	0019740	biological_process	nitrogen utilization
E	1901704	biological_process	L-glutamine biosynthetic process
F	0003824	molecular_function	catalytic activity
F	0004356	molecular_function	glutamine synthetase activity
F	0005737	cellular_component	cytoplasm
F	0016020	cellular_component	membrane
F	0019740	biological_process	nitrogen utilization
F	1901704	biological_process	L-glutamine biosynthetic process

Functional Information from PROSITE/UniProt

site_id	PS00181
Number of Residues	16
Details	GLNA_ATP Glutamine synthetase putative ATP-binding region signature. KPLygd..NGSGmHthvS

Chain	Residue	Details
A	LYS268-SER283

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	504
Details	Domain: {"description":"GS beta-grasp","evidences":[{"source":"PROSITE-ProRule","id":"PRU01330","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2202
Details	Domain: {"description":"GS catalytic","evidences":[{"source":"PROSITE-ProRule","id":"PRU01331","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	48
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P9WN39","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	36
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P0A1P6","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P12425","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P77961","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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